FMO DATABASE

FMODB ID: LN679

Calculation Name: 1QGV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1QGV

Chain ID: A

ChEMBL ID:

UniProt ID: P83876

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	135
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1348799.974544
FMO2-HF: Nuclear repulsion	1291467.170492
FMO2-HF: Total energy	-57332.804052
FMO2-MP2: Total energy	-57495.088962

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
0.305	1.943	0	-0.764	-0.873	0.002

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.029 / q_NPA : -0.029

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	4	MET	0	-0.055	-0.009	3.697	0.575	1.977	-0.001	-0.713	-0.687	0.002
4	A	5	LEU	0	-0.003	0.007	6.158	-0.090	-0.090	0.000	0.000	0.000	0.000
5	A	6	PRO	0	-0.033	-0.010	3.703	-0.382	-0.146	0.001	-0.051	-0.186	0.000
6	A	7	HIS	0	0.044	0.004	6.385	-0.182	-0.182	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.098	-0.038	8.172	0.129	0.129	0.000	0.000	0.000	0.000
8	A	9	HIS	0	0.001	-0.036	9.184	0.047	0.047	0.000	0.000	0.000	0.000
9	A	10	ASN	0	-0.018	-0.007	12.579	-0.053	-0.053	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.105	0.047	15.029	0.009	0.009	0.000	0.000	0.000	0.000
11	A	12	TRP	0	-0.039	-0.014	12.496	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	13	GLN	0	0.026	0.004	10.181	0.045	0.045	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.027	0.023	12.207	-0.013	-0.013	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.914	-0.961	14.251	-0.020	-0.020	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.018	-0.021	12.447	-0.005	-0.005	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.004	0.009	10.835	-0.041	-0.041	0.000	0.000	0.000	0.000
17	A	18	ILE	0	-0.065	-0.033	12.062	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.035	-0.015	15.605	-0.005	-0.005	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.103	-0.039	11.789	-0.032	-0.032	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.806	-0.860	11.163	-0.048	-0.048	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.923	-0.956	15.045	-0.065	-0.065	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.894	-0.946	17.096	0.019	0.019	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.713	0.825	9.357	-0.118	-0.118	0.000	0.000	0.000	0.000
24	A	25	VAL	0	-0.069	-0.027	16.466	-0.019	-0.019	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.040	0.020	12.794	0.029	0.029	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.055	-0.040	13.838	-0.016	-0.016	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.025	0.002	13.471	0.034	0.034	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.745	0.836	14.570	-0.235	-0.235	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.021	-0.004	16.070	0.014	0.014	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.038	-0.013	18.668	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	32	HIS	0	0.009	0.012	19.162	0.011	0.011	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.750	-0.868	15.182	0.194	0.194	0.000	0.000	0.000	0.000
33	A	34	TRP	0	-0.067	-0.030	18.164	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	35	ASP	-1	-0.763	-0.883	21.236	0.093	0.093	0.000	0.000	0.000	0.000
35	A	36	PRO	0	-0.005	-0.014	22.131	0.009	0.009	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.067	-0.034	23.370	0.005	0.005	0.000	0.000	0.000	0.000
37	A	38	CYS	0	-0.005	0.018	18.561	0.019	0.019	0.000	0.000	0.000	0.000
38	A	39	MET	0	-0.021	0.013	18.367	0.016	0.016	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.926	0.954	18.771	-0.091	-0.091	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.030	-0.006	17.796	0.018	0.018	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.751	-0.860	14.455	0.264	0.264	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.964	-0.967	14.608	0.207	0.207	0.000	0.000	0.000	0.000
43	A	44	VAL	0	-0.005	-0.001	16.402	0.034	0.034	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.027	0.004	13.566	0.027	0.027	0.000	0.000	0.000	0.000
45	A	46	TYR	0	0.041	0.016	9.369	0.102	0.102	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.076	-0.038	12.623	0.055	0.055	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.103	-0.063	14.793	-0.017	-0.017	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.065	0.037	9.883	-0.018	-0.018	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.818	-0.910	9.462	1.132	1.132	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.849	0.925	12.428	-0.264	-0.264	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.012	-0.004	13.833	-0.045	-0.045	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.892	0.947	8.517	-1.230	-1.230	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.049	-0.026	12.939	-0.025	-0.025	0.000	0.000	0.000	0.000
54	A	55	PHE	0	-0.017	-0.018	15.766	-0.035	-0.035	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.007	0.002	14.568	-0.034	-0.034	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.006	0.015	8.583	0.079	0.079	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.035	-0.021	9.839	-0.064	-0.064	0.000	0.000	0.000	0.000
58	A	59	TYR	0	0.020	0.008	6.791	0.046	0.046	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.023	0.000	10.430	-0.056	-0.056	0.000	0.000	0.000	0.000
60	A	61	VAL	0	0.032	0.011	11.921	0.031	0.031	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.718	-0.860	14.567	0.102	0.102	0.000	0.000	0.000	0.000
62	A	63	ILE	0	-0.036	-0.027	16.899	-0.007	-0.007	0.000	0.000	0.000	0.000
63	A	64	THR	0	-0.058	-0.022	20.026	-0.017	-0.017	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.940	-0.954	14.280	0.178	0.178	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.076	-0.035	15.143	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	67	PRO	0	0.007	-0.002	18.549	0.001	0.001	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.901	-0.961	20.094	0.055	0.055	0.000	0.000	0.000	0.000
68	A	69	PHE	0	0.015	-0.008	17.766	-0.007	-0.007	0.000	0.000	0.000	0.000
69	A	70	ASN	0	0.032	0.037	22.675	0.008	0.008	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.807	0.913	24.895	-0.041	-0.041	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.093	-0.048	21.609	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	73	TYR	0	0.003	-0.007	21.627	0.003	0.003	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.834	-0.929	26.649	0.042	0.042	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.020	-0.006	24.614	-0.002	-0.002	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.005	-0.011	26.187	-0.001	-0.001	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.895	-0.938	25.829	0.065	0.065	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.045	-0.020	25.117	0.006	0.006	0.000	0.000	0.000	0.000
78	A	80	THR	0	-0.051	-0.013	21.581	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.010	0.011	17.432	0.013	0.013	0.000	0.000	0.000	0.000
80	A	82	MET	0	-0.056	-0.015	18.779	-0.020	-0.020	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.033	0.002	18.285	0.016	0.016	0.000	0.000	0.000	0.000
82	A	84	PHE	0	0.055	0.030	17.581	-0.018	-0.018	0.000	0.000	0.000	0.000
83	A	85	PHE	0	-0.020	-0.016	18.497	0.006	0.006	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.862	0.912	19.686	-0.019	-0.019	0.000	0.000	0.000	0.000
85	A	87	ASN	0	0.051	0.022	19.621	-0.003	-0.003	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.895	0.979	21.297	-0.034	-0.034	0.000	0.000	0.000	0.000
87	A	89	HIS	0	0.007	0.002	22.475	0.000	0.000	0.000	0.000	0.000	0.000
88	A	90	ILE	0	-0.099	-0.062	22.598	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	91	MET	0	0.026	0.018	24.476	0.006	0.006	0.000	0.000	0.000	0.000
90	A	92	ILE	0	0.006	-0.017	23.369	0.000	0.000	0.000	0.000	0.000	0.000
91	A	93	ASP	-1	-0.864	-0.920	27.975	0.053	0.053	0.000	0.000	0.000	0.000
92	A	94	LEU	0	0.001	-0.020	27.517	0.002	0.002	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.004	0.006	31.509	0.000	0.000	0.000	0.000	0.000	0.000
94	A	96	THR	0	0.019	-0.005	32.662	-0.002	-0.002	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.006	0.009	35.293	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	98	ASN	0	-0.008	0.012	28.737	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.041	-0.033	30.645	0.002	0.002	0.000	0.000	0.000	0.000
98	A	100	ASN	0	0.009	0.005	25.183	-0.006	-0.006	0.000	0.000	0.000	0.000
99	A	101	LYN	0	-0.003	0.017	23.510	0.009	0.009	0.000	0.000	0.000	0.000
100	A	102	ILE	0	0.014	0.001	22.294	-0.002	-0.002	0.000	0.000	0.000	0.000
101	A	103	ASN	0	-0.015	-0.010	23.064	0.010	0.010	0.000	0.000	0.000	0.000
102	A	104	TRP	0	0.019	0.020	25.068	-0.004	-0.004	0.000	0.000	0.000	0.000
103	A	105	ALA	0	0.009	0.010	23.188	0.008	0.008	0.000	0.000	0.000	0.000
104	A	106	MET	0	-0.033	0.005	22.786	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.858	-0.934	23.801	0.110	0.110	0.000	0.000	0.000	0.000
106	A	108	ASP	-1	-0.904	-0.949	24.130	0.126	0.126	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.936	0.960	18.235	-0.255	-0.255	0.000	0.000	0.000	0.000
108	A	110	GLN	0	-0.010	-0.028	21.039	0.026	0.026	0.000	0.000	0.000	0.000
109	A	111	GLU	-1	-0.787	-0.901	23.326	0.103	0.103	0.000	0.000	0.000	0.000
110	A	112	MET	0	0.063	0.015	18.251	-0.005	-0.005	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.084	-0.039	18.744	0.006	0.006	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.852	-0.912	20.486	0.118	0.118	0.000	0.000	0.000	0.000
113	A	115	ILE	0	-0.023	0.008	22.402	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	116	ILE	0	0.044	0.024	16.312	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.872	-0.920	20.257	0.113	0.113	0.000	0.000	0.000	0.000
116	A	118	THR	0	-0.066	-0.047	21.981	-0.018	-0.018	0.000	0.000	0.000	0.000
117	A	119	VAL	0	0.005	-0.005	21.602	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	120	TYR	0	0.038	0.029	19.896	-0.012	-0.012	0.000	0.000	0.000	0.000
119	A	121	ARG	1	0.807	0.883	21.928	-0.105	-0.105	0.000	0.000	0.000	0.000
120	A	122	GLY	0	-0.024	-0.013	25.178	-0.010	-0.010	0.000	0.000	0.000	0.000
121	A	123	ALA	0	0.034	0.009	23.190	-0.008	-0.008	0.000	0.000	0.000	0.000
122	A	124	ARG	1	0.906	0.963	23.104	-0.078	-0.078	0.000	0.000	0.000	0.000
123	A	125	LYS	1	0.849	0.932	25.120	-0.056	-0.056	0.000	0.000	0.000	0.000
124	A	126	GLY	0	0.025	0.011	27.808	-0.004	-0.004	0.000	0.000	0.000	0.000
125	A	127	ARG	1	0.874	0.951	28.791	-0.046	-0.046	0.000	0.000	0.000	0.000
126	A	128	GLY	0	0.029	0.003	27.538	0.002	0.002	0.000	0.000	0.000	0.000
127	A	129	LEU	0	0.007	0.017	28.384	0.002	0.002	0.000	0.000	0.000	0.000
128	A	130	VAL	0	-0.069	-0.039	25.855	-0.003	-0.003	0.000	0.000	0.000	0.000
129	A	131	VAL	0	0.025	0.010	29.209	0.001	0.001	0.000	0.000	0.000	0.000
130	A	132	SER	0	-0.015	-0.013	27.998	0.005	0.005	0.000	0.000	0.000	0.000
131	A	133	PRO	0	-0.010	-0.015	30.102	0.001	0.001	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.865	0.947	27.002	-0.095	-0.095	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.918	-0.946	32.758	0.051	0.051	0.000	0.000	0.000	0.000
134	A	136	TYR	0	-0.027	-0.011	30.834	-0.003	-0.003	0.000	0.000	0.000	0.000
135	A	137	SER	0	-0.024	-0.003	37.739	-0.003	-0.003	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)